ID A0A1J0GV28_9CAUD Unreviewed; 584 AA.
AC A0A1J0GV28;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=vBVspPpVa5_0035 {ECO:0000313|EMBL:APC46027.1};
OS Vibrio phage vB_VspP_pVa5.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Schitoviridae; Pontosvirinae; Galateavirus; Galateavirus PVA5.
OX NCBI_TaxID=1913109 {ECO:0000313|EMBL:APC46027.1, ECO:0000313|Proteomes:UP000225978};
RN [1] {ECO:0000313|EMBL:APC46027.1, ECO:0000313|Proteomes:UP000225978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28531104;
RA Kalatzis P.G., Rorbo N.I., Castillo D., Mauritzen J.J., Jorgensen J.,
RA Kokkari C., Zhang F., Katharios P., Middelboe M.;
RT "Stumbling across the Same Phage: Comparative Genomics of Widespread
RT Temperate Phages Infecting the Fish Pathogen Vibrio anguillarum.";
RL Viruses 9:E122-E122(2017).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; KX889068; APC46027.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000225978; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000225978}.
FT DOMAIN 12..74
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 81..389
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 397..555
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 584 AA; 65334 MW; 668E9F4056CE543C CRC64;
MEIKLNRDKL MSEQGRKLVV DYYLQGEEKS PQEAFARACK FFATDDAHAQ RLYDHVSQLH
FMFSSPILSN AGDGNKGMPI SCFLSYVPDS VEGLIKHGEE TRWLSVLGGG VGGHWDAVRA
VSDKSPGPIP FIHDIDGAMT AYKQGQTRKG AYAAYLDVGH PDIEEFITSR TPTGGDINRK
NFNSHHAVNL TNDFMRHVYA DWDWELKCPH SKRVTKTIKA RALWESILET RHRTGEPFLN
FIDTANDALH PVQKKLGLKI HGSNLCNEIH LVTDEQRTAV CCLASLNLEK YDDWKNTGLV
GDLVELLDNV LQYFIDIAPD AVSKAKYAAM RSRDIGIGAM GWHGYLMQKS IAFESTEANR
ETYKIFRRIK EAAVARSQQL AVEKGSCPDA QEAGQVVRNL HLLAIAPNAN SSAICNATAS
IEPIKSNAFA HRTRAGTDLI VNKYLVALLN SHIPPTLTIL GKSEQSWVDE QITSVIQNKG
SVQHLDYLSD HEKLVFKTFE EIDQHYVIDQ AGIRQDFLCQ GQSVNLSFPA EVPKSYVNSV
HLSAYERRLK GLYYLRTTSI KQVNITDVVA KDKADDEECT QCHA
//
